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Database: UniProt
Entry: A0A1I3FLV4_9ACTN
LinkDB: A0A1I3FLV4_9ACTN
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ID   A0A1I3FLV4_9ACTN        Unreviewed;       414 AA.
AC   A0A1I3FLV4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Tryptophan synthase beta chain {ECO:0000256|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00133};
GN   Name=trpB {ECO:0000256|HAMAP-Rule:MF_00133};
GN   ORFNames=SAMN05216561_10534 {ECO:0000313|EMBL:SFI11911.1};
OS   Nocardioides psychrotolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1005945 {ECO:0000313|EMBL:SFI11911.1, ECO:0000313|Proteomes:UP000198649};
RN   [1] {ECO:0000313|EMBL:SFI11911.1, ECO:0000313|Proteomes:UP000198649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.11156 {ECO:0000313|EMBL:SFI11911.1,
RC   ECO:0000313|Proteomes:UP000198649};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000256|HAMAP-Rule:MF_00133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC         glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC         Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00000003, ECO:0000256|HAMAP-
CC         Rule:MF_00133};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00133};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC       ECO:0000256|HAMAP-Rule:MF_00133}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|ARBA:ARBA00011270, ECO:0000256|HAMAP-Rule:MF_00133}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|ARBA:ARBA00009982,
CC       ECO:0000256|HAMAP-Rule:MF_00133}.
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DR   EMBL; FOQG01000005; SFI11911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3FLV4; -.
DR   STRING; 1005945.SAMN05216561_10534; -.
DR   OrthoDB; 9766131at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000198649; Unassembled WGS sequence.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06446; Trp-synth_B; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00263; trpB; 1.
DR   PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR   PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00133};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00133};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00133};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00133}; Reference proteome {ECO:0000313|Proteomes:UP000198649};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00133}.
FT   DOMAIN          74..399
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         105
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   414 AA;  43963 MW;  C526ABDFC222AA38 CRC64;
     MTTTSTPGQQ APVIPPSSFD ADEGGWFGDF GGRFMPEALV AALDELTEAW QDAMADPTFI
     HDFETICRDY GGMPSSLYEA RRLSDKVGAR ILLKREDLNH TGAHKIRNVL GQALLTRRMG
     KQRVIAETGA GQHGVASATA AAYFGLDCTV YMGAVDVKRQ ALNVARMHLL GAKVVPVDSG
     SATLKDAINE AMRDWVASVD HTAYLFGTAA GPHPFPSMVR DFARGIGDEA RAQCLERYGR
     LPDAIAACVG GGSNAIGLFQ AFLDDEDVAI YGFEPGGDGI ETGRHAATIH QGDSGVLHGA
     RTYVLQDEDG QTIESHSISA GLDYPGVGPQ HAHLAKVGRA TYLPITDAEA MDAMALLSRT
     EGIIPAIESA HAIAGALRVA EQLGAEKGPD ATVLINLSGR GDKDMETAME WFDL
//
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